Structural basis for detoxification and oxidative stress protection in membranes

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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Structural basis for detoxification and oxidative stress protection in membranes. / Holm, Peter; Bhakat, Priyaranjan; Jegerschold, Caroline; Gyobu, Nobuhiko; Mitsuoka, Kaoru; Fujiyoshi, Yoshinori; Morgenstern, Ralf; Hebert, Hans.

I: Journal of Molecular Biology, Vol. 360, Nr. 5, 2006, s. 934-945.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Harvard

Holm, P, Bhakat, P, Jegerschold, C, Gyobu, N, Mitsuoka, K, Fujiyoshi, Y, Morgenstern, R & Hebert, H 2006, 'Structural basis for detoxification and oxidative stress protection in membranes', Journal of Molecular Biology, vol. 360, nr. 5, s. 934-945. https://doi.org/10.1016/j.jmb.2006.05.056

APA

Holm, P., Bhakat, P., Jegerschold, C., Gyobu, N., Mitsuoka, K., Fujiyoshi, Y., ... Hebert, H. (2006). Structural basis for detoxification and oxidative stress protection in membranes. Journal of Molecular Biology, 360(5), 934-945. https://doi.org/10.1016/j.jmb.2006.05.056

CBE

Holm P, Bhakat P, Jegerschold C, Gyobu N, Mitsuoka K, Fujiyoshi Y, Morgenstern R, Hebert H. 2006. Structural basis for detoxification and oxidative stress protection in membranes. Journal of Molecular Biology. 360(5):934-945. https://doi.org/10.1016/j.jmb.2006.05.056

MLA

Vancouver

Author

Holm, Peter ; Bhakat, Priyaranjan ; Jegerschold, Caroline ; Gyobu, Nobuhiko ; Mitsuoka, Kaoru ; Fujiyoshi, Yoshinori ; Morgenstern, Ralf ; Hebert, Hans. / Structural basis for detoxification and oxidative stress protection in membranes. I: Journal of Molecular Biology. 2006 ; Vol. 360, Nr. 5. s. 934-945.

RIS

TY - JOUR

T1 - Structural basis for detoxification and oxidative stress protection in membranes

AU - Holm, Peter

AU - Bhakat, Priyaranjan

AU - Jegerschold, Caroline

AU - Gyobu, Nobuhiko

AU - Mitsuoka, Kaoru

AU - Fujiyoshi, Yoshinori

AU - Morgenstern, Ralf

AU - Hebert, Hans

PY - 2006

Y1 - 2006

N2 - Synthesis of mediators of fever, pain and inflammation as well as protection against reactive molecules and oxidative stress is a hallmark of the MAPEG superfamily (membrane associated proteins in eicosanoid and glutathione metabolism). The structure of a MAPEG member, rat mictosomal glutathione transferase 1, at 3.2 angstrom resolution, solved here in complex with glutathione by electron crystallography, defines the active site location and a cytosolic domain involved in enzyme activation. The glutathione binding site is found to be different from that of the canonical soluble glutathione transferases. The architecture of the homotrimer supports a catalytic mechanism involving subunit interactions and reveals both cytosolic and membraneous substrate entry sites, providing a rationale for the membrane location of the enzyme.

AB - Synthesis of mediators of fever, pain and inflammation as well as protection against reactive molecules and oxidative stress is a hallmark of the MAPEG superfamily (membrane associated proteins in eicosanoid and glutathione metabolism). The structure of a MAPEG member, rat mictosomal glutathione transferase 1, at 3.2 angstrom resolution, solved here in complex with glutathione by electron crystallography, defines the active site location and a cytosolic domain involved in enzyme activation. The glutathione binding site is found to be different from that of the canonical soluble glutathione transferases. The architecture of the homotrimer supports a catalytic mechanism involving subunit interactions and reveals both cytosolic and membraneous substrate entry sites, providing a rationale for the membrane location of the enzyme.

KW - electron crystallography

KW - protein structure

KW - enzymology

KW - membrane protein

KW - oxidative stress

U2 - 10.1016/j.jmb.2006.05.056

DO - 10.1016/j.jmb.2006.05.056

M3 - Article

VL - 360

SP - 934

EP - 945

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 1089-8638

IS - 5

ER -